MEH1_YEAST
ID MEH1_YEAST Reviewed; 184 AA.
AC Q02205; D6VX73;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Protein MEH1;
DE AltName: Full=EGO complex subunit 1;
DE AltName: Full=GSE complex subunit 2;
GN Name=MEH1; Synonyms=EGO1, GSE2; OrderedLocusNames=YKR007W; ORFNames=YK106;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1441752; DOI=10.1002/yea.320080908;
RA Duesterhoeft A., Philippsen P.;
RT "DNA sequencing and analysis of a 24.7 kb segment encompassing centromere
RT CEN11 of Saccharomyces cerevisiae reveals nine previously unknown open
RT reading frames.";
RL Yeast 8:749-759(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP FUNCTION, IDENTIFICATION IN THE EGO COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=15989961; DOI=10.1016/j.molcel.2005.05.020;
RA Dubouloz F., Deloche O., Wanke V., Cameroni E., De Virgilio C.;
RT "The TOR and EGO protein complexes orchestrate microautophagy in yeast.";
RL Mol. Cell 19:15-26(2005).
RN [6]
RP PALMITOYLATION AT CYS-7 AND CYS-8.
RX PubMed=16751107; DOI=10.1016/j.cell.2006.03.042;
RA Roth A.F., Wan J., Bailey A.O., Sun B., Kuchar J.A., Green W.N.,
RA Phinney B.S., Yates J.R. III, Davis N.G.;
RT "Global analysis of protein palmitoylation in yeast.";
RL Cell 125:1003-1013(2006).
RN [7]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE GSE
RP COMPLEX, AND MYRISTOYLATION AT GLY-2.
RX PubMed=16732272; DOI=10.1038/ncb1419;
RA Gao M., Kaiser C.A.;
RT "A conserved GTPase-containing complex is required for intracellular
RT sorting of the general amino-acid permease in yeast.";
RL Nat. Cell Biol. 8:657-667(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146 AND SER-149, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146 AND SER-149, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [11]
RP DISRUPTION PHENOTYPE.
RX PubMed=29698392; DOI=10.1371/journal.pgen.1007334;
RA Ukai H., Araki Y., Kira S., Oikawa Y., May A.I., Noda T.;
RT "Gtr/Ego-independent TORC1 activation is achieved through a glutamine-
RT sensitive interaction with Pib2 on the vacuolar membrane.";
RL PLoS Genet. 14:e1007334-e1007334(2018).
RN [12]
RP DISRUPTION PHENOTYPE.
RX PubMed=32801125; DOI=10.1242/jcs.245555;
RA Uemura S., Mochizuki T., Amemiya K., Kurosaka G., Yazawa M., Nakamoto K.,
RA Ishikawa Y., Izawa S., Abe F.;
RT "Amino acid homeostatic control by TORC1 in Saccharomyces cerevisiae under
RT high hydrostatic pressure.";
RL J. Cell Sci. 133:jcs245555-jcs245555(2020).
CC -!- FUNCTION: Component of the GSE complex, a GTPase complex required for
CC intracellular sorting of GAP1 out of the endosome (PubMed:16732272).
CC Component of the EGO complex, a complex involved in the regulation of
CC microautophagy (PubMed:15989961). {ECO:0000269|PubMed:15989961,
CC ECO:0000269|PubMed:16732272}.
CC -!- SUBUNIT: Component of the GSE complex composed of GTR1, GTR2, SLM4,
CC MEH1 and LTV1. Component of the EGO complex, at least composed of GTR2,
CC SLM4 and MEH1. {ECO:0000269|PubMed:15989961,
CC ECO:0000269|PubMed:16732272}.
CC -!- INTERACTION:
CC Q02205; Q00582: GTR1; NbExp=3; IntAct=EBI-27062, EBI-7954;
CC Q02205; P38247: SLM4; NbExp=4; IntAct=EBI-27062, EBI-21507;
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:15989961}.
CC -!- DISRUPTION PHENOTYPE: Abnormal activation of TORC1 signaling during
CC high hydrostatic pressure (mechanical stress) (PubMed:32801125).
CC Abnormal punctate localization of TOR1 (PubMed:32801125). Increases
CC cellular levels of glutamine and alanine during high hydrostatic
CC pressure (mechanical stress) (PubMed:32801125). Sensitive to rapamycin
CC and high hydrostatic pressure (mechanical stress) (PubMed:29698392,
CC PubMed:32801125). Simultaneous disruption of PIB2 results in loss of
CC viability (PubMed:29698392). {ECO:0000269|PubMed:29698392,
CC ECO:0000269|PubMed:32801125}.
CC -!- MISCELLANEOUS: Present with 2740 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X65124; CAA46245.1; -; Genomic_DNA.
DR EMBL; Z28232; CAA82077.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09163.1; -; Genomic_DNA.
DR PIR; S25815; S25815.
DR RefSeq; NP_012932.1; NM_001179797.1.
DR PDB; 4XPM; X-ray; 2.40 A; A=146-184.
DR PDB; 6JWP; X-ray; 3.20 A; C/H=33-184.
DR PDBsum; 4XPM; -.
DR PDBsum; 6JWP; -.
DR AlphaFoldDB; Q02205; -.
DR SMR; Q02205; -.
DR BioGRID; 34139; 348.
DR ComplexPortal; CPX-3172; EGO complex.
DR ComplexPortal; CPX-3233; GSE complex.
DR DIP; DIP-1922N; -.
DR IntAct; Q02205; 14.
DR MINT; Q02205; -.
DR STRING; 4932.YKR007W; -.
DR iPTMnet; Q02205; -.
DR SwissPalm; Q02205; -.
DR MaxQB; Q02205; -.
DR PaxDb; Q02205; -.
DR PRIDE; Q02205; -.
DR EnsemblFungi; YKR007W_mRNA; YKR007W; YKR007W.
DR GeneID; 853876; -.
DR KEGG; sce:YKR007W; -.
DR SGD; S000001715; MEH1.
DR VEuPathDB; FungiDB:YKR007W; -.
DR eggNOG; ENOG502S74H; Eukaryota.
DR HOGENOM; CLU_136947_0_0_1; -.
DR InParanoid; Q02205; -.
DR OMA; TKETRGH; -.
DR BioCyc; YEAST:G3O-31985-MON; -.
DR PRO; PR:Q02205; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; Q02205; protein.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0005770; C:late endosome; IDA:ComplexPortal.
DR GO; GO:0031902; C:late endosome membrane; IDA:SGD.
DR GO; GO:0071986; C:Ragulator complex; IDA:SGD.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:InterPro.
DR GO; GO:0042632; P:cholesterol homeostasis; IEA:InterPro.
DR GO; GO:0032456; P:endocytic recycling; IDA:ComplexPortal.
DR GO; GO:0016237; P:lysosomal microautophagy; IMP:SGD.
DR GO; GO:0007040; P:lysosome organization; IEA:InterPro.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:InterPro.
DR GO; GO:0032008; P:positive regulation of TOR signaling; IC:ComplexPortal.
DR GO; GO:0072665; P:protein localization to vacuole; IMP:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0001919; P:regulation of receptor recycling; IEA:InterPro.
DR GO; GO:0007035; P:vacuolar acidification; IMP:SGD.
DR InterPro; IPR028209; LAMTOR1/MEH1.
DR Pfam; PF15454; LAMTOR; 1.
DR SMART; SM01262; LAMTOR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autophagy; Coiled coil; Lipoprotein; Membrane; Myristate;
KW Palmitate; Phosphoprotein; Protein transport; Reference proteome;
KW Transport; Vacuole.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT CHAIN 2..184
FT /note="Protein MEH1"
FT /id="PRO_0000203193"
FT REGION 89..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 30..71
FT /evidence="ECO:0000255"
FT COMPBIAS 92..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000305|PubMed:16732272"
FT LIPID 7
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:16751107"
FT LIPID 8
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:16751107"
FT HELIX 44..70
FT /evidence="ECO:0007829|PDB:6JWP"
FT HELIX 74..79
FT /evidence="ECO:0007829|PDB:6JWP"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:6JWP"
FT HELIX 88..93
FT /evidence="ECO:0007829|PDB:6JWP"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:6JWP"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:6JWP"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:4XPM"
FT HELIX 154..171
FT /evidence="ECO:0007829|PDB:4XPM"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:4XPM"
SQ SEQUENCE 184 AA; 20242 MW; 995DD1E68331D050 CRC64;
MGAVLSCCRN HSGEENEALL REQQAGYGSQ GNANDEYDAE QMRLKEHEHE QKLLAREQEL
RDIVANTNDK LIDISMINNS GIVIQGTDLQ EALDKRQQEE GGDSREDERS AGDDNLSGHS
VPSSGSAQAT THQTAPRTNT FTLLTSPDSA KISKEQLKKL HSNILNEIFS QSQVNKPGPL
TVPF
